KL41B_DANRE
ID KL41B_DANRE Reviewed; 605 AA.
AC F1QEG2; Q7SYD2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Kelch-like protein 41b;
DE AltName: Full=Kelch repeat and BTB domain-containing protein 10b;
GN Name=klhl41b {ECO:0000312|ZFIN:ZDB-GENE-030131-9875};
GN Synonyms=kbtbd10b {ECO:0000312|ZFIN:ZDB-GENE-030131-9875};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=24268659; DOI=10.1016/j.ajhg.2013.10.020;
RA Gupta V.A., Ravenscroft G., Shaheen R., Todd E.J., Swanson L.C., Shiina M.,
RA Ogata K., Hsu C., Clarke N.F., Darras B.T., Farrar M.A., Hashem A.,
RA Manton N.D., Muntoni F., North K.N., Sandaradura S.A., Nishino I.,
RA Hayashi Y.K., Sewry C.A., Thompson E.M., Yau K.S., Brownstein C.A.,
RA Yu T.W., Allcock R.J., Davis M.R., Wallgren-Pettersson C., Matsumoto N.,
RA Alkuraya F.S., Laing N.G., Beggs A.H.;
RT "Identification of KLHL41 mutations implicates BTB-Kelch-mediated
RT ubiquitination as an alternate pathway to myofibrillar disruption in
RT nemaline myopathy.";
RL Am. J. Hum. Genet. 93:1108-1117(2013).
CC -!- FUNCTION: Involved in skeletal muscle development and maintenance.
CC {ECO:0000269|PubMed:24268659}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60662}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A2AUC9}. Sarcoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O60662}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O60662}.
CC -!- DEVELOPMENTAL STAGE: Expression is predominantly seen in striated
CC muscles, and strong expression in heart and skeletal muscles is
CC observed throughout development to at least 5 dpf.
CC {ECO:0000269|PubMed:24268659}.
CC -!- DISRUPTION PHENOTYPE: Knockdown of klhl41b result in reduced
CC disorganized muscle without any other significant abnormalities.
CC Knockdown of both genes (klhl41a and klhl41b) is lethal by 3 dpf.
CC Double knockdown fish exhibit severely disorganized muscle compared to
CC controls and either of the single knockdowns.
CC {ECO:0000269|PubMed:24268659}.
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DR EMBL; CABZ01067487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054912; AAH54912.1; -; mRNA.
DR RefSeq; NP_945330.1; NM_198979.1.
DR AlphaFoldDB; F1QEG2; -.
DR SMR; F1QEG2; -.
DR STRING; 7955.ENSDARP00000012238; -.
DR PaxDb; F1QEG2; -.
DR PRIDE; F1QEG2; -.
DR Ensembl; ENSDART00000013588; ENSDARP00000012238; ENSDARG00000006757.
DR GeneID; 321064; -.
DR KEGG; dre:321064; -.
DR CTD; 321064; -.
DR ZFIN; ZDB-GENE-030131-9875; klhl41b.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000158859; -.
DR HOGENOM; CLU_004253_14_4_1; -.
DR InParanoid; F1QEG2; -.
DR OMA; FQSYFFQ; -.
DR OrthoDB; 946131at2759; -.
DR PhylomeDB; F1QEG2; -.
DR TreeFam; TF351653; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:F1QEG2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000006757; Expressed in muscle tissue and 21 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045214; P:sarcomere organization; IMP:ZFIN.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:InterPro.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:ZFIN.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030571; KLHL41.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR24412:SF146; PTHR24412:SF146; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Kelch repeat; Membrane;
KW Reference proteome; Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..605
FT /note="Kelch-like protein 41b"
FT /id="PRO_0000431066"
FT DOMAIN 32..102
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 136..238
FT /note="BACK"
FT /evidence="ECO:0000255"
FT REPEAT 345..397
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 398..446
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 447..494
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 496..541
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 543..598
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT CONFLICT 181
FT /note="L -> S (in Ref. 2; AAH54912)"
FT CONFLICT 266
FT /note="E -> K (in Ref. 2; AAH54912)"
SQ SEQUENCE 605 AA; 68713 MW; EE2AF594C3C0558A CRC64;
MDPKAIKEEL RLFQSTLLQD GLKELLNENK FVDCTLKIGD RCFPCHRLIM AACSPYFREL
FFSEDGKEKD IGKEVVLDDV DPNIMDMILQ YLYSAEIDLV DDNVQEIFAV ANRFQIPSVF
TVCVNYLQQK LSMANCLAVF RLGLVLSVPR LAIAARDFIA DRFETVSSEE EFLQLAPHEL
LALIGGDMLN VEKEEVVFES VMKWVRNDKA NRVKSLAEAF DCIRFRLLPE KYFREKVETD
DIIKGDPELL KKLQLVKDAF KGKLPEKKPK EKKEGEVNGE EEGEEMLPGF LNDNRRLGMY
GRDLIVMIND TAAVAYDVVE NECFLAAMAE QVPKNHVSLC TKKNQLFIVG GLFVDEESKE
SPLQCYFYQL DSFSSDWRAL PPMPSPRCLF NLGESENLLF AIAGKDLQTN ESLDSVMCFD
TERMKWSETK KLPLHIHGHS VVSHNNLVYC IGGKTDDNKA LSKMFVYNHK QSEWRELASM
KTPRAMFGAV VHKGKIIVTG GVNEDGLTAL SETYDFDTNK WDTFTEFPQE RSSVNLVSSG
GNLFSIGGFA IVELEDKNIG PSEITDIWQY EEDKKTWSGM LREMRYASGS SCVGMRLNAA
RMPKL
